Structure and function of chitin deacetylases

Daan van Aalten

Author address: 

Wellcome Trust Biocentre, School of Life Sciences Univ. of Dundee, Dundee DD1 5EH, UK


Chitinases are enzymes that catalyze the hydrolysis of the β (1,4)-glycosidic bonds between the {sl N}-acetyl-D-glucosamine (GlcNAc) monomers of chitin. Within the family 18 chitinases two subfamilies exist, the extensively studied bacterial-type chitinases and the less well studied plant-type chitinases with as prototype hevamine from {sl Hevea brasiliensis}. Both classes of enzymes are found in the genomes of yeast and fungi. Whereas the bacterial-type family 18 chitinases are non-essential, genetic data on the plant-type family 18 chitinases points to a role in cell wall morphology. For example, disruption of Aspergillus nidulans chiA leads to a defect in germination and hyphal growth, whereas the Saccharomyces cerevisiae chitinase 1 CTS1 plays a key role in separation of mother and daughter cells at the end of cell division. Specific inhibitors of these enzymes would be useful as tools to study their role in cell wall morphogenesis and could possess anti-fungal properties. Progress towards understanding the structure/mechanism of these chitinases will be described, together with screening-based discovery of inhibitors.

abstract No: 


Full conference title: 

The First International Fungal / Plant Cell Wall Meeting
    • International Fungal / Plant Cell Wall Meeting 1st